IFH1_YEAST - dbPTM
IFH1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID IFH1_YEAST
UniProt AC P39520
Protein Name Protein IFH1
Gene Name IFH1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 1085
Subcellular Localization Nucleus .
Protein Description Controls the pre-rRNA processing machinery in conjunction with FHL1. Could convert FHL1 from a repressor to an activator..
Protein Sequence MAGKKSPRKSTINHSTHSGKLPANIKRLIKKGESDTKSRQSPPTLSTTRPRRFSLIYSSESSLSDVSDSDKNKSTNPHKIKRKAKNISNNSQGKKSKLIQRQIDNDDEGTESSDYQAVTDGEESENEEEESEEEEEDDDEDDDDDDDDGSDSDSDSETSSDDENIDFVKLTAQRKKRAMKALSAMNTNSNTLYSSRENSNKNKSVKLSPKKENEEEQKEEKEKEKEEQQKQQESNKKEVNGSGTTTTQQALSFKFKKEDDGISFGNGNEGYNEDIGEEVLDLKNKENNGNEEDKLDSKVMLGNNDELRFPNISESDESEYDIDQDAYFDVINNEDSHGEIGTDLETGEDDLPILEEEEQNIVSELQNDDELSFDGSIHEEGSDPVEDAENKFLQNEYNQENGYDEEDDEEDEIMSDFDMPFYEDPKFANLYYYGDGSEPKLSLSTSLPLMLNDEKLSKLKKKEAKKREQEERKQRRKLYKKTQKPSTRTTSNVDNDEYIFNVFFQSDDENSGHKSKKGRHKSGKSHIEHKNKGSNLIKSNDDLEPSTHSTVLNSGKYDSSDDEYDNILLDVAHMPSDDECSESETSHDADTDEELRALDSDSLDIGTELDDDYEDDDDDSSVTNVFIDIDDLDPDSFYFHYDSDGSSSLISSNSDKENSDGSKDCKHDLLETVVYVDDESTDEDDNLPPPSSRSKNIGSKAKEIVSSNVVGLRPPKLGTWETDNKPFSIIDGLSTKSLYALIQEHQQLREQHQRAQTPDVKREGSSNGNNGDELTLNELLNMSELEDDSPSHTDDMENNYNDAINSKSTNGHAADWYEVPKVPLSAFRNKGINAYEEDEYMIPANSNRKVPIGYIGNERTRKKIDKMKELQRKKTEKKRQLKKKKKLLKIRKQRQKAIKEQETMNLQLGINGHEIIGNNNSHSDINTGTDFTTNENTPMNELPSHAPEDASLIPHNSDLAVDSNTRKNSTKSVGLDEIHEILGKDENDLLSVGDINGYDAQEGHVIEDTDADILASLTAPVQFDNTLSHENSNSMWRRRQSMVEAAAENLRFTKNGLFSESALADIEGIMGNDVNHSFEFNDVLQ
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
6Phosphorylation--MAGKKSPRKSTIN
--CCCCCCCCCCCCC		33.1630377154
9AcetylationAGKKSPRKSTINHST
CCCCCCCCCCCCCCC		56.1624489116
20AcetylationNHSTHSGKLPANIKR
CCCCCCCCCCHHHHH		55.0724489116
26AcetylationGKLPANIKRLIKKGE
CCCCHHHHHHHHCCC		40.7425381059
38PhosphorylationKGESDTKSRQSPPTL
CCCCCCCCCCCCCCC		37.3330377154
41PhosphorylationSDTKSRQSPPTLSTT
CCCCCCCCCCCCCCC		31.5630377154
44PhosphorylationKSRQSPPTLSTTRPR
CCCCCCCCCCCCCCC		36.4030377154
83AcetylationNPHKIKRKAKNISNN
CHHHHHHHHHHCCCC		59.7225381059
85AcetylationHKIKRKAKNISNNSQ
HHHHHHHHHCCCCCC		58.8225381059
91PhosphorylationAKNISNNSQGKKSKL
HHHCCCCCCCHHHHH		44.5630377154
94AcetylationISNNSQGKKSKLIQR
CCCCCCCHHHHHHHH		46.3525381059
95AcetylationSNNSQGKKSKLIQRQ
CCCCCCHHHHHHHHH		60.7025381059
97AcetylationNSQGKKSKLIQRQID
CCCCHHHHHHHHHCC		59.4925381059
180AcetylationQRKKRAMKALSAMNT
HHHHHHHHHHHHHCC		45.2324489116
180UbiquitinationQRKKRAMKALSAMNT
HHHHHHHHHHHHHCC		45.2317644757
183PhosphorylationKRAMKALSAMNTNSN
HHHHHHHHHHCCCCC		30.2619823750
187PhosphorylationKALSAMNTNSNTLYS
HHHHHHCCCCCCCCC		27.2622369663
189PhosphorylationLSAMNTNSNTLYSSR
HHHHCCCCCCCCCCC		29.2022369663
191PhosphorylationAMNTNSNTLYSSREN
HHCCCCCCCCCCCCC		27.2222369663
193PhosphorylationNTNSNTLYSSRENSN
CCCCCCCCCCCCCCC		11.5422369663
194PhosphorylationTNSNTLYSSRENSNK
CCCCCCCCCCCCCCC		26.4920377248
195PhosphorylationNSNTLYSSRENSNKN
CCCCCCCCCCCCCCC		30.0121440633
199PhosphorylationLYSSRENSNKNKSVK
CCCCCCCCCCCCCCC		44.4122369663
208PhosphorylationKNKSVKLSPKKENEE
CCCCCCCCCCCCCHH		29.0225533186
234PhosphorylationEQQKQQESNKKEVNG
HHHHHHHHHCCCCCC		50.0030377154
236AcetylationQKQQESNKKEVNGSG
HHHHHHHCCCCCCCC		60.6424489116
254AcetylationTQQALSFKFKKEDDG
HHHHHEECEEECCCC		53.5524489116
256AcetylationQALSFKFKKEDDGIS
HHHEECEEECCCCCC		56.7124489116
426UbiquitinationMPFYEDPKFANLYYY
CCCCCCCCCCCEEEE		70.2317644757
440UbiquitinationYGDGSEPKLSLSTSL
ECCCCCCCCCCCCCC		46.8117644757
446PhosphorylationPKLSLSTSLPLMLND
CCCCCCCCCCCCCCH		25.3121440633
489PhosphorylationTQKPSTRTTSNVDND
HCCCCCCCCCCCCCC		34.3622369663
490PhosphorylationQKPSTRTTSNVDNDE
CCCCCCCCCCCCCCC		18.2722369663
491PhosphorylationKPSTRTTSNVDNDEY
CCCCCCCCCCCCCCE		33.9522369663
498PhosphorylationSNVDNDEYIFNVFFQ
CCCCCCCEEEEEEEE		17.4222369663
506PhosphorylationIFNVFFQSDDENSGH
EEEEEEECCCCCCCC		41.7022369663
511PhosphorylationFQSDDENSGHKSKKG
EECCCCCCCCCCCCC		39.9822369663
524AcetylationKGRHKSGKSHIEHKN
CCCCCCCCCCCCCCC		46.0525381059
534PhosphorylationIEHKNKGSNLIKSND
CCCCCCCCCCCCCCC		30.0330377154
539PhosphorylationKGSNLIKSNDDLEPS
CCCCCCCCCCCCCCC		38.2022369663
725UbiquitinationGTWETDNKPFSIIDG
CCCCCCCCCCCEEEC		50.6923749301
734PhosphorylationFSIIDGLSTKSLYAL
CCEEECCCHHHHHHH		39.0421440633
735PhosphorylationSIIDGLSTKSLYALI
CEEECCCHHHHHHHH		29.6922369663
736UbiquitinationIIDGLSTKSLYALIQ
EEECCCHHHHHHHHH		34.7823749301
757PhosphorylationEQHQRAQTPDVKREG
HHHHHHCCCCCCCCC		22.0721082442
807UbiquitinationYNDAINSKSTNGHAA
CHHHHHCCCCCCCCC		57.7317644757
821UbiquitinationADWYEVPKVPLSAFR
CCCCCCCCCCHHHHH		62.7523749301
830UbiquitinationPLSAFRNKGINAYEE
CHHHHHCCCCCCCCC		57.8423749301
849UbiquitinationIPANSNRKVPIGYIG
ECCCCCCCCCCCCCC		57.5223749301
972PhosphorylationTRKNSTKSVGLDEIH
CCCCCCCCCCHHHHH		22.8522369663
1041PhosphorylationSMWRRRQSMVEAAAE
HHHHHHHHHHHHHHH		24.0025704821
1077PhosphorylationMGNDVNHSFEFNDVL
CCCCCCCCCCCCCCC		22.6728889911
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of IFH1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of IFH1_YEAST !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of IFH1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FHL1_YEASTFHL1physical
15692568
FHL1_YEASTFHL1genetic
7785326
SRL1_YEASTSRL1physical
11283351
UTP22_YEASTUTP22physical
17452446
PTH2_YEASTPTH2genetic
19061648
SNF12_YEASTSNF12physical
20059977
EPL1_YEASTEPL1physical
20059977
ADA2_YEASTADA2physical
20059977
EAF6_YEASTEAF6physical
20059977
TAF4_YEASTTAF4physical
20059977
MED6_YEASTMED6physical
20059977
UTP22_YEASTUTP22physical
27818142
RRP7_YEASTRRP7physical
27818142
CSK22_YEASTCKA2physical
27818142
CSK21_YEASTCKA1physical
27818142
CSK2B_YEASTCKB1physical
27818142
CSK2C_YEASTCKB2physical
27818142
UTP22_YEASTUTP22genetic
27818142
FHL1_YEASTFHL1physical
27321754
CSK2B_YEASTCKB1physical
27321754
CSK2C_YEASTCKB2physical
27321754
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of IFH1_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A multidimensional chromatography technology for in-depthphosphoproteome analysis.";
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
Mol. Cell. Proteomics 7:1389-1396(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-757 AND SER-1077, ANDMASS SPECTROMETRY.
"Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases.";
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.;
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-208 AND THR-757, ANDMASS SPECTROMETRY.
"Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry.";
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-208, AND MASSSPECTROMETRY.

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